ID TRPC_CORGL Reviewed; 474 AA. AC P06560; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 26-JUL-2002, sequence version 2. DT 16-JUN-2009, entry version 75. DE RecName: Full=Tryptophan biosynthesis protein trpCF; DE Includes: DE RecName: Full=Indole-3-glycerol phosphate synthase; DE Short=IGPS; DE EC=4.1.1.48; DE Includes: DE RecName: Full=N-(5'-phospho-ribosyl)anthranilate isomerase; DE Short=PRAI; DE EC=5.3.1.24; GN Name=trpC; Synonyms=trpCF; OrderedLocusNames=Cgl3033, cg3362; OS Corynebacterium glutamicum (Brevibacterium flavum). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=1718; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=87117512; PubMed=3808947; DOI=10.1093/nar/14.24.10113; RA Matsui K., Sano K., Ohtsubo E.; RT "Complete nucleotide and deduced amino acid sequences of the RT Brevibacterium lactofermentum tryptophan operon."; RL Nucleic Acids Res. 14:10113-10114(1986). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025; RA Nakagawa S.; RT "Complete genomic sequence of Corynebacterium glutamicum ATCC 13032."; RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025; RX MEDLINE=22830012; PubMed=12948626; DOI=10.1016/S0168-1656(03)00154-8; RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., RA Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., RA Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., RA McHardy A.C., Meyer F., Moeckel B., Pfefferle W., Puehler A., RA Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., RA Tauch A.; RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence RT and its impact on the production of L-aspartate-derived amino acids RT and vitamins."; RL J. Biotechnol. 104:5-25(2003). CC -!- FUNCTION: Bifunctional enzyme that catalyzes two sequential steps CC of tryptophan biosynthetic pathway. The first reaction is CC catalyzed by the isomerase, coded by the trpF domain; the second CC reaction is catalyzed by the synthase, coded by the trpC domain. CC -!- CATALYTIC ACTIVITY: N-(5-phospho-beta-D-ribosyl)anthranilate = 1- CC (2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate. CC -!- CATALYTIC ACTIVITY: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5- CC phosphate = 1-C-(3-indolyl)-glycerol 3-phosphate + CO(2) + H(2)O. CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 3/5. CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 4/5. CC -!- SUBUNIT: Monomer. CC -!- SIMILARITY: In the N-terminal section; belongs to the trpC family. CC -!- SIMILARITY: In the C-terminal section; belongs to the trpF family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X04960; CAA28626.1; -; Genomic_DNA. DR EMBL; BA000036; BAC00427.1; -; Genomic_DNA. DR EMBL; BX927157; CAF18973.1; -; Genomic_DNA. DR PIR; E24723; E24723. DR RefSeq; NP_602226.2; -. DR RefSeq; YP_227283.1; -. DR HSSP; P00909; 1JCM. DR GeneID; 1020975; -. DR GeneID; 3345646; -. DR GenomeReviews; BA000036_GR; Cgl3033. DR GenomeReviews; BX927147_GR; cg3362. DR KEGG; cgb:cg3362; -. DR HOGENOM; P06560; -. DR OMA; P06560; YILECKK. DR BioCyc; CGLU196627-1:CG3362-MON; -. DR BRENDA; 4.1.1.48; 812. DR BRENDA; 5.3.1.24; 812. DR GO; GO:0004425; F:indole-3-glycerol-phosphate synthase activity; IEA:HAMAP. DR GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IEA:HAMAP. DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:HAMAP. DR HAMAP; MF_00134; fused; 1. DR HAMAP; MF_00135; fused; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013798; Indole-3-glycerol_P_synth. DR InterPro; IPR001468; Indole-3-GPS_central. DR InterPro; IPR001240; PRAI. DR Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1. DR Pfam; PF00218; IGPS; 1. DR Pfam; PF00697; PRAI; 1. DR ProDom; PD001511; IGPS; 1. DR PROSITE; PS00614; IGPS; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Complete proteome; Decarboxylase; Isomerase; Lyase; KW Multifunctional enzyme; Tryptophan biosynthesis. FT CHAIN 1 474 Tryptophan biosynthesis protein trpCF. FT /FTId=PRO_0000154276. FT REGION 1 262 Indole-3-glycerol phosphate synthase. FT REGION 263 474 N-(5'-phosphoribosyl)anthranilate FT isomerase. FT CONFLICT 88 89 SG -> AA (in Ref. 1; CAA28626). FT CONFLICT 110 110 A -> G (in Ref. 1; CAA28626). FT CONFLICT 130 131 HA -> RP (in Ref. 1; CAA28626). FT CONFLICT 153 153 A -> D (in Ref. 1; CAA28626). FT CONFLICT 302 302 L -> S (in Ref. 1; CAA28626). FT CONFLICT 343 343 D -> G (in Ref. 1; CAA28626). FT CONFLICT 381 383 Missing (in Ref. 1; CAA28626). FT CONFLICT 454 474 AGAKDAGALLKIFATISTFHY -> GWGERCRRAAENFRDH FT LHIPLLKV (in Ref. 1; CAA28626). SQ SEQUENCE 474 AA; 50477 MW; C347C7016BB97F9A CRC64; MTSNNLPTVL ESIVEGRRGH LEEIRARIAH VDVDALPKST RSLFDSLNQG RGGARFIMEC KSASPSLGMI REHYQPGEIA RVYSRYASGI SVLCEPDRFG GDYDHLATVA ATSHLPVLCK DFIIDPVQVH AARYFGADAI LLMLSVLDDE EYAALAAEAA RFDLDILTEV IDEEEVARAI KLGAKIFGVN HRNLHDLSID LDRSRRLSKL IPADAVLVSE SGVRDTETVR QLGGHSNAFL VGSQLTSQEN VDLAARELVY GPNKVCGLTS PSAAQTARAA GAVYGGLIFE EASPRNVSRE TLQKIIAAEP NLRYVAVSRR TSGYKDLLVD GIFAVQIHAP LQDSVEAEKA LIAAVREEVG PQVQVWRAIS MSSPLGAEVA AAVEGDVDKL ILDAHEGGSG EVFDWATVPA AVKAKSLLAG GISPDNAAQA LAVGCAGLDI NSGVEYPAGA GTWAGAKDAG ALLKIFATIS TFHY //